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The protein having 37kda has 336.36 amino acids long, roughly making single-stranded alpha-helix 93.43 turns, giving it a rise in 504.4 Â (Armstrong).

A secondary structure component, an alpha helix, has an amino acid chain organised in a spiral. The following characteristics describe the perfect alpha helix:

  • It is a right-handed helix that completes one turn every 3.6 residues, rises by about 5.4 with each turn, and is often somewhat curved.
  • Hydrogen bonds hold it together between the C=O of residue I and the NH of residue I+4.
  • The (phi, psi) angles of all residues involved in an alpha-helix are comparable.
  • These angles, around -60 and -50, are taken from the Ramachandran plot's bottom left quadrant.

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